CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity

Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic a...

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Published in:Biochemical Engineering Journal
Main Authors: Guauque Torres, María del Pilar, Foresti, María Laura, Ferreira, Maria Lujan
Format: Article in Journal/Newspaper
Language:English
Published: Elsevier
Subjects:
Online Access:http://hdl.handle.net/11336/6549
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author Guauque Torres, María del Pilar
Foresti, María Laura
Ferreira, Maria Lujan
author_facet Guauque Torres, María del Pilar
Foresti, María Laura
Ferreira, Maria Lujan
author_sort Guauque Torres, María del Pilar
collection CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas)
container_start_page 36
container_title Biochemical Engineering Journal
container_volume 90
description Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic activity in three different test reactions: esterification of oleic acid and ethanol in absence of solvents, esterification of oleic acid and heptanol in organic medium, and hydrolysis of triolein in emulsioned medium. The impact of the cross-linker/protein mass ratio on CLEAs activity, and its evolution with storage time were evaluated in the solventless synthesis of ethyloleate. The amount of cross-linker used showed to be a key parameter for the evolution of the catalytic activity of CLEAs during storage. Under the best conditions found, hyperactivated CALB CLEAs with up to 188% of recovered activity in ethyl oleate synthesis were obtained. In terms of hydrolytic activity mature layered CALB CLEAs showed a retained activity of 68%. The assay of dried mature layered CALB CLEAs in heptyl oleate synthesis showed catalytic activities much higher than the one exhibited by free CALB, reaching 1 h-fatty acid conversions of 14% and 2%, respectively. The high catalytic activity shown by layered CALB CLEAs, suggests that they are an interesting alternative specially for the catalysis of fatty acid esterifications in both organic and solventless medium. Fil: Guauque Torres, María del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina Fil: Ferreira, Maria Lujan. ...
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op_doi https://doi.org/10.1016/j.bej.2014.05.004
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http://hdl.handle.net/11336/6549
Guauque Torres, María del Pilar; Foresti, María Laura; Ferreira, Maria Lujan; CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity; Elsevier; Biochemical Engineering Journal; 90; 5-2014; 36-43
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spelling ftconicet:oai:ri.conicet.gov.ar:11336/6549 2025-01-16T19:04:44+00:00 CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity Guauque Torres, María del Pilar Foresti, María Laura Ferreira, Maria Lujan application/pdf http://hdl.handle.net/11336/6549 eng eng Elsevier info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1369703X14001193 info:eu-repo/semantics/altIdentifier/doi/ info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bej.2014.05.004 http://hdl.handle.net/11336/6549 Guauque Torres, María del Pilar; Foresti, María Laura; Ferreira, Maria Lujan; CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity; Elsevier; Biochemical Engineering Journal; 90; 5-2014; 36-43 1369-703X info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-nd/2.5/ar/ Lipase Immobilization Cleas Cofeeder Core https://purl.org/becyt/ford/2.4 https://purl.org/becyt/ford/2 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1016/j.bej.2014.05.004 2023-09-24T19:59:52Z Highly active CALB cross-linked enzyme aggregates (CLEAs) were synthesized using a layered methodology based on the synthesis of a cross-linked protein cofeeder core over which an external layer of lipase was later cross-linked. The layered CALB CLEAs were characterized in terms of their catalytic activity in three different test reactions: esterification of oleic acid and ethanol in absence of solvents, esterification of oleic acid and heptanol in organic medium, and hydrolysis of triolein in emulsioned medium. The impact of the cross-linker/protein mass ratio on CLEAs activity, and its evolution with storage time were evaluated in the solventless synthesis of ethyloleate. The amount of cross-linker used showed to be a key parameter for the evolution of the catalytic activity of CLEAs during storage. Under the best conditions found, hyperactivated CALB CLEAs with up to 188% of recovered activity in ethyl oleate synthesis were obtained. In terms of hydrolytic activity mature layered CALB CLEAs showed a retained activity of 68%. The assay of dried mature layered CALB CLEAs in heptyl oleate synthesis showed catalytic activities much higher than the one exhibited by free CALB, reaching 1 h-fatty acid conversions of 14% and 2%, respectively. The high catalytic activity shown by layered CALB CLEAs, suggests that they are an interesting alternative specially for the catalysis of fatty acid esterifications in both organic and solventless medium. Fil: Guauque Torres, María del Pilar. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina Fil: Foresti, María Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Bahía Blanca. Planta Piloto de Ingeniería Química (i); Argentina. Consejo Nacional de Investigaciones Cientificas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Tecnologia En Polimeros y Nanotecnologia; Argentina Fil: Ferreira, Maria Lujan. ... Article in Journal/Newspaper Antarc* Antarctica CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Argentina Ferreira ENVELOPE(-62.050,-62.050,-64.600,-64.600) Biochemical Engineering Journal 90 36 43
spellingShingle Lipase
Immobilization
Cleas
Cofeeder Core
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
Guauque Torres, María del Pilar
Foresti, María Laura
Ferreira, Maria Lujan
CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title_full CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title_fullStr CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title_full_unstemmed CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title_short CLEAs of Candida antarctica lipase B (CALB) with a bovine serum albumin (BSA) cofeeder core. Study of their catalytic activity
title_sort cleas of candida antarctica lipase b (calb) with a bovine serum albumin (bsa) cofeeder core. study of their catalytic activity
topic Lipase
Immobilization
Cleas
Cofeeder Core
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
topic_facet Lipase
Immobilization
Cleas
Cofeeder Core
https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
url http://hdl.handle.net/11336/6549